1q03

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Revision as of 19:42, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1q03" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q03, resolution 2.05Å" /> '''Crystal structure o...)
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File:1q03.gif


1q03, resolution 2.05Å

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Crystal structure of FGF-1, S50G/V51G mutant

OverviewOverview

The beta-turn is the most common type of nonrepetitive structure in, globular proteins, comprising ~25% of all residues; however, a detailed, understanding of effects of specific residues upon beta-turn stability and, conformation is lacking. Human acidic fibroblast growth factor (FGF-1) is, a member of the beta-trefoil superfold and contains a total of five, beta-hairpin structures (antiparallel beta-sheets connected by a reverse, turn). beta-Turns related by the characteristic threefold structural, symmetry of this superfold exhibit different primary structures, and in, some cases, different secondary structures. As such, they represent a, useful system with which to study the role that turn sequences play in, determining structure, stability, and folding of the protein. Two turns, related by the threefold structural symmetry, the beta4/beta5 and, beta8/beta9 turns, were subjected to both sequence-swapping and, poly-glycine substitution mutations, and the effects upon stability, folding, and structure were investigated. In the wild-type protein these, turns are of identical length, but exhibit different conformations. These, conformations were observed to be retained during sequence-swapping and, glycine substitution mutagenesis. The results indicate that the beta-turn, structure at these positions is not determined by the turn sequence., Structural analysis suggests that residues flanking the turn are a primary, structural determinant of the conformation within the turn.

DiseaseDisease

Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], LADD syndrome OMIM:[602115]

About this StructureAbout this Structure

1Q03 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor., Kim J, Lee J, Brych SR, Logan TM, Blaber M, Protein Sci. 2005 Feb;14(2):351-9. Epub 2005 Jan 4. PMID:15632285

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